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Related Concept Videos

Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
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Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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Protein sorting at the trans-Golgi network.

Yusong Guo1, Daniel W Sirkis, Randy Schekman

  • 1Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, California 94720-3200;

Annual Review of Cell and Developmental Biology
|August 24, 2014
PubMed
Summary
This summary is machine-generated.

The trans-Golgi network (TGN) sorts cellular proteins into transport carriers. This review details the molecular machinery and mechanisms ensuring accurate protein sorting for cell function and disease.

Keywords:
Arfscargo adaptorscargo receptorsphospholipidsvesicle coat proteins

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Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • The trans-Golgi network (TGN) acts as a critical sorting hub for newly synthesized proteins.
  • Efficient protein transport relies on complex machinery to package cargo into specific carriers.

Purpose of the Study:

  • To review the cytosolic and transmembrane sorting machinery at the TGN.
  • To describe molecular interactions and regulatory mechanisms governing TGN protein sorting.
  • To highlight the physiological and pathological relevance of TGN sorting.

Main Methods:

  • Literature review of TGN protein sorting mechanisms.
  • Analysis of molecular interactions involved in cargo capture and carrier formation.
  • Examination of regulatory pathways controlling TGN sorting fidelity.

Main Results:

  • Detailed overview of the protein sorting machinery operating at the TGN.
  • Elucidation of molecular interactions essential for distinguishing and packaging cargo.
  • Identification of regulatory mechanisms ensuring accurate protein transport.

Conclusions:

  • Accurate protein sorting at the TGN is crucial for cellular function.
  • Dysregulation of TGN sorting machinery contributes to various diseases.
  • Understanding TGN sorting provides insights into fundamental cell biology and disease pathogenesis.